BRENDA - Enzyme Database

Proline dehydrogenase regulates redox state and respiratory metabolism in Trypanosoma cruzi

Paes, L.S.; Suarez Mantilla, B.; Zimbres, F.M.; Pral, E.M.; Diogo de Melo, P.; Tahara, E.B.; Kowaltowski, A.J.; Elias, M.C.; Silber, A.M.; PLoS ONE 8, e69419 (2013)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
1.5.5.2
gene Tc00.1047053506411.30, sequence comparisons, recombinant expression of the active His6-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3) cells, reverse transcription PCR (RT-PCR) and quantitative real-time PCR (qRT-PCR) expression analysis, functional complementation of ProDH-deficient, PUT1 mutant Saccharomyces cerevisiae strain YLR142W. TcPRODH gene expression in the mutant diminishes free intracellular proline levels and an enhances sensitivity to oxidative stress
Trypanosoma cruzi
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.5.5.2
0.01658
-
L-proline
recombinant enzyme, pH 7.5, 37°C, with 2,6-dichlorphenol-indophenol
Trypanosoma cruzi
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.5.5.2
mitochondrial inner membrane
TcPRODH is associated with the mitochondrial inner membrane, identification of a predicted N-terminal mitochondrial targeting signal, followed by a putative transmembrane alpha helix spanning domain
Trypanosoma cruzi
5743
-
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.5.5.2
L-proline + a quinone
Trypanosoma cruzi
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
ir
1.5.5.2
L-proline + a quinone
Trypanosoma cruzi CL Brener
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
ir
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.5.5.2
Trypanosoma cruzi
Q4CVA1
-
-
1.5.5.2
Trypanosoma cruzi CL Brener
Q4CVA1
-
-
Purification (Commentary)
EC Number
Commentary
Organism
1.5.5.2
recombinant active His6-tagged enzyme from Escherichia coli strain BL21-CodonPlus (DE3) by nickel affinity chromatography
Trypanosoma cruzi
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
1.5.5.2
epimastigote
TcPRODH mRNA and protein expression are strongly upregulated in the intracellular epimastigote, a stage which requires an external supply of proline
Trypanosoma cruzi
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.5.5.2
L-proline + 2,6-dichlorphenol-indophenol
-
743635
Trypanosoma cruzi
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
1.5.5.2
L-proline + 2,6-dichlorphenol-indophenol
-
743635
Trypanosoma cruzi CL Brener
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
1.5.5.2
L-proline + a quinone
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
743635
Trypanosoma cruzi
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
-
ir
1.5.5.2
L-proline + a quinone
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
743635
Trypanosoma cruzi CL Brener
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
-
ir
1.5.5.2
L-proline + cytochrome c
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
743635
Trypanosoma cruzi
(S)-1-pyrroline-5-carboxylate + reduced cytochrome c
-
-
-
ir
1.5.5.2
L-proline + cytochrome c
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
743635
Trypanosoma cruzi CL Brener
(S)-1-pyrroline-5-carboxylate + reduced cytochrome c
-
-
-
ir
1.5.5.2
L-proline + NAD+
NADP+ is a poor electron acceptor
743635
Trypanosoma cruzi
(S)-1-pyrroline-5-carboxylate + NADH
-
-
-
?
1.5.5.2
L-proline + NAD+
NADP+ is a poor electron acceptor
743635
Trypanosoma cruzi CL Brener
(S)-1-pyrroline-5-carboxylate + NADH
-
-
-
?
1.5.5.2
additional information
poor activity with D-proline, hydroxyproline, L-pipecolic acid, nicotinic acid, and thiazolidine-4-carboxylic acid
743635
Trypanosoma cruzi
?
-
-
-
-
1.5.5.2
additional information
poor activity with D-proline, hydroxyproline, L-pipecolic acid, nicotinic acid, and thiazolidine-4-carboxylic acid
743635
Trypanosoma cruzi CL Brener
?
-
-
-
-
Subunits
EC Number
Subunits
Commentary
Organism
1.5.5.2
dimer
-
Trypanosoma cruzi
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.5.5.2
37
-
recombinant enzyme
Trypanosoma cruzi
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.5.5.2
7.5
-
recombinant enzyme
Trypanosoma cruzi
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.5.5.2
cytochrome c
-
Trypanosoma cruzi
1.5.5.2
FAD
TcPRODH is a FAD-dependent protein, key residues involved in cofactor (FAD) binding are Arg431 and Glu559
Trypanosoma cruzi
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.5.5.2
gene Tc00.1047053506411.30, sequence comparisons, recombinant expression of the active His6-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3) cells, reverse transcription PCR (RT-PCR) and quantitative real-time PCR (qRT-PCR) expression analysis, functional complementation of ProDH-deficient, PUT1 mutant Saccharomyces cerevisiae strain YLR142W. TcPRODH gene expression in the mutant diminishes free intracellular proline levels and an enhances sensitivity to oxidative stress
Trypanosoma cruzi
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.5.5.2
cytochrome c
-
Trypanosoma cruzi
1.5.5.2
FAD
TcPRODH is a FAD-dependent protein, key residues involved in cofactor (FAD) binding are Arg431 and Glu559
Trypanosoma cruzi
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.5.5.2
0.01658
-
L-proline
recombinant enzyme, pH 7.5, 37°C, with 2,6-dichlorphenol-indophenol
Trypanosoma cruzi
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.5.5.2
mitochondrial inner membrane
TcPRODH is associated with the mitochondrial inner membrane, identification of a predicted N-terminal mitochondrial targeting signal, followed by a putative transmembrane alpha helix spanning domain
Trypanosoma cruzi
5743
-
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.5.5.2
L-proline + a quinone
Trypanosoma cruzi
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
ir
1.5.5.2
L-proline + a quinone
Trypanosoma cruzi CL Brener
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
ir
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.5.5.2
recombinant active His6-tagged enzyme from Escherichia coli strain BL21-CodonPlus (DE3) by nickel affinity chromatography
Trypanosoma cruzi
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
1.5.5.2
epimastigote
TcPRODH mRNA and protein expression are strongly upregulated in the intracellular epimastigote, a stage which requires an external supply of proline
Trypanosoma cruzi
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.5.5.2
L-proline + 2,6-dichlorphenol-indophenol
-
743635
Trypanosoma cruzi
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
1.5.5.2
L-proline + 2,6-dichlorphenol-indophenol
-
743635
Trypanosoma cruzi CL Brener
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
1.5.5.2
L-proline + a quinone
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
743635
Trypanosoma cruzi
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
-
ir
1.5.5.2
L-proline + a quinone
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
743635
Trypanosoma cruzi CL Brener
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
-
ir
1.5.5.2
L-proline + cytochrome c
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
743635
Trypanosoma cruzi
(S)-1-pyrroline-5-carboxylate + reduced cytochrome c
-
-
-
ir
1.5.5.2
L-proline + cytochrome c
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
743635
Trypanosoma cruzi CL Brener
(S)-1-pyrroline-5-carboxylate + reduced cytochrome c
-
-
-
ir
1.5.5.2
L-proline + NAD+
NADP+ is a poor electron acceptor
743635
Trypanosoma cruzi
(S)-1-pyrroline-5-carboxylate + NADH
-
-
-
?
1.5.5.2
L-proline + NAD+
NADP+ is a poor electron acceptor
743635
Trypanosoma cruzi CL Brener
(S)-1-pyrroline-5-carboxylate + NADH
-
-
-
?
1.5.5.2
additional information
poor activity with D-proline, hydroxyproline, L-pipecolic acid, nicotinic acid, and thiazolidine-4-carboxylic acid
743635
Trypanosoma cruzi
?
-
-
-
-
1.5.5.2
additional information
poor activity with D-proline, hydroxyproline, L-pipecolic acid, nicotinic acid, and thiazolidine-4-carboxylic acid
743635
Trypanosoma cruzi CL Brener
?
-
-
-
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.5.5.2
dimer
-
Trypanosoma cruzi
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.5.5.2
37
-
recombinant enzyme
Trypanosoma cruzi
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.5.5.2
7.5
-
recombinant enzyme
Trypanosoma cruzi
Expression
EC Number
Organism
Commentary
Expression
1.5.5.2
Trypanosoma cruzi
TcPRODH mRNA and protein expression are strongly upregulated in the intracellular epimastigote, a stage which requires an external supply of proline
up
General Information
EC Number
General Information
Commentary
Organism
1.5.5.2
additional information
key residues involved in substrate binding are Asp370, Tyr 540, Arg555, Arg556, and Leu513
Trypanosoma cruzi
1.5.5.2
physiological function
in trypanosomatids, L-proline is involved in a number of key processes, including energy metabolism, resistance to oxidative and nutritional stress and osmoregulation. In addition, this amino acid supports critical parasite life cycle processes by acting as an energy source, thus enabling host-cell invasion by the parasite and subsequent parasite differentiation. Proline dehydrogenase regulates redox state and respiratory metabolism in Trypanosoma cruzi, free proline accumulation constitutes a defense against oxidative imbalance
Trypanosoma cruzi
General Information (protein specific)
EC Number
General Information
Commentary
Organism
1.5.5.2
additional information
key residues involved in substrate binding are Asp370, Tyr 540, Arg555, Arg556, and Leu513
Trypanosoma cruzi
1.5.5.2
physiological function
in trypanosomatids, L-proline is involved in a number of key processes, including energy metabolism, resistance to oxidative and nutritional stress and osmoregulation. In addition, this amino acid supports critical parasite life cycle processes by acting as an energy source, thus enabling host-cell invasion by the parasite and subsequent parasite differentiation. Proline dehydrogenase regulates redox state and respiratory metabolism in Trypanosoma cruzi, free proline accumulation constitutes a defense against oxidative imbalance
Trypanosoma cruzi
Expression (protein specific)
EC Number
Organism
Commentary
Expression
1.5.5.2
Trypanosoma cruzi
TcPRODH mRNA and protein expression are strongly upregulated in the intracellular epimastigote, a stage which requires an external supply of proline
up